1V8Z

X-ray crystal structure of the Tryptophan Synthase b2 Subunit from Hyperthermophile, Pyrococcus furiosus

1V8Z の概要

• エントリーDOI: 10.2210/pdb1v8z/pdb
• 関連するPDBエントリー: 1GEQ
• 分子名称: Tryptophan synthase beta chain 1, SODIUM ION, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: beta+alpha, riken structural genomics/proteomics initiative, rsgi, structural genomics, lyase
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 171400.68

構造登録者

Hioki, Y.,Ogasahara, K.,Lee, S.J.,Ma, J.,Ishida, M.,Yamagata, Y.,Matsuura, Y.,Ota, M.,Kuramitsu, S.,Yutani, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-01-15, 公開日: 2005-02-22, 最終更新日: 2023-10-25)

主引用文献

Hioki, Y.,Ogasahara, K.,Lee, S.J.,Ma, J.,Ishida, M.,Yamagata, Y.,Matsuura, Y.,Ota, M.,Ikeguchi, M.,Kuramitsu, S.,Yutani, K.
The crystal structure of the tryptophan synthase beta subunit from the hyperthermophile Pyrococcus furiosus. Investigation of stabilization factors
Eur.J.Biochem., 271:2624-2635, 2004

PubMed Abstract: The structure of the tryptophan synthase beta2 subunit (Pfbeta2) from the hyperthermophile, Pyrococcus furiosus, was determined by X-ray crystallographic analysis at 2.2 A resolution, and its stability was examined by DSC. This is the first report of the X-ray structure of the tryptophan synthase beta2 subunit alone, although the structure of the tryptophan synthase alpha2beta2 complex from Salmonella typhimurium has already been reported. The structure of Pfbeta2 was essentially similar to that of the beta2 subunit (Stbeta2) in the alpha2beta2 complex from S. typhimurium. The sequence alignment with secondary structures of Pfbeta and Stbeta in monomeric form showed that six residues in the N-terminal region and three residues in the C-terminal region were deleted in Pfbeta, and one residue at Pro366 of Stbeta and at Ile63 of Pfbeta was inserted. The denaturation temperature of Pfbeta2 was higher by 35 degrees C than the reported values from mesophiles at approximately pH 8. On the basis of structural information on both proteins, the analyses of the contributions of each stabilization factor indicate that: (a) the higher stability of Pfbeta2 is not caused by either a hydrophobic interaction or an increase in ion pairs; (b) the number of hydrogen bonds involved in the main chains of Pfbeta is greater by about 10% than that of Stbeta, indicating that the secondary structures of Pfbeta are more stabilized than those of Stbeta and (c) the sequence of Pfbeta seems to be better fitted to an ideally stable structure than that of Stbeta, as assessed from X-ray structure data.

PubMed: 15206928
DOI: 10.1111/j.1432-1033.2004.04191.x

実験手法

X-RAY DIFFRACTION (2.21 Å)